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Crystal structure of CYCLO(L-leucyl-L-phenylalanyl) synthase

Analyse Crystal structure of CYCLO(L-leucyl-L-phenylalanyl) synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4Q24
Type
protein
Length
224 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CYCLO(L-leucyl-L-phenylalanyl) synthase
EC
2.3.2.20
UniProt
Q8GED7
Ligands
XVE
Pockets
1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACYCLO(L-leucyl-L-phenylalanyl) synthase (EC 2.3.2.20)protein22458% helix, 15% strandQ8GED7

Ligands and binding sites

  • XVE · Phenylmethyl N-[(2S)-4-chloro-3-oxo-1-phenyl-butan-2-yl]carbamate · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13400.750.8643XVE

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 4Q24 · Crystal structure of Cyclo(L-leucyl-L-phenylalanyl) synthase · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8GED7 · AlphaFold monomer V2.0 prediction for CYCLO(L-leucyl-L-phenylalanyl) synthase (Q8GED7) · a predicted model of the same protein · chain A against A, TM-score 0.99

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